1y29

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y29 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y29 OCA], [http://www.ebi.ac.uk/pdbsum/1y29 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y29 RCSB]</span>
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Revision as of 21:57, 30 March 2008


PDB ID 1y29

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Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Three dimensional solution structure of huwentoxin-x by 2D 1H-NMR


Overview

Huwentoxin-X (HWTX-X) is a novel peptide toxin, purified from the venom of the spider Ornithoctonus huwena. It comprises 28 amino acid residues including six cysteine residues as disulfide bridges linked in the pattern of I-IV, II-V, and III-VI. Its cDNA, determined by rapid amplification of 3' and 5' cDNA ends, encodes a 65-residue prepropeptide. HWTX-X shares low sequence homology with omega-conotoxins GVIA and MVIIA, two well known blockers of N-type Ca2+ channels. Nevertheless, whole cell studies indicate that it can block N-type Ca2+ channels in rat dorsal root ganglion cells (IC50 40 nm) and the blockage by HWTX-X is completely reversible. The rank order of specificity for N-type Ca2+ channels is GVIA approximately HWTX-X > MVIIA. In contrast to GVIA and MVIIA, HWTX-X had no detectable effect on the twitch response of rat vas deferens to low frequency electrical stimulation, indicating that HWTX-X has different selectivity for isoforms of N-type Ca2+ channels, compared with GVIA or MVIIA. A comparison of the structures of HWTX-X and GVIA reveals that they not only adopt a common structural motif (inhibitor cystine knot), but also have a similar functional motif, a binding surface formed by the critical residue Tyr, and several basic residues. However, the dissimilarities of their binding surfaces provide some insights into their different selectivities for isoforms of N-type Ca2+ channels.

About this Structure

1Y29 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Function and solution structure of Huwentoxin-X, a specific blocker of N-type calcium channels, from the Chinese bird spider Ornithoctonus huwena., Liu Z, Dai J, Dai L, Deng M, Hu Z, Hu W, Liang S, J Biol Chem. 2006 Mar 31;281(13):8628-35. Epub 2006 Jan 26. PMID:16439354

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